A0A2J7PNA5 · A0A2J7PNA5_9NEOP

Function

function

Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.

Activity regulation

Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity.

Pathway

Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site12-14substrate
Binding site40-44substrate
Binding site131ATP (UniProtKB | ChEBI)
Binding site167-172ATP (UniProtKB | ChEBI)
Binding site188ATP (UniProtKB | ChEBI)
Binding site195K+ (UniProtKB | ChEBI)
Binding site197K+ (UniProtKB | ChEBI)
Binding site200-201ATP (UniProtKB | ChEBI)
Active site201Proton acceptor
Binding site201substrate
Binding site233K+ (UniProtKB | ChEBI)
Binding site236K+ (UniProtKB | ChEBI)
Binding site238K+ (UniProtKB | ChEBI)
Binding site242K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionribokinase activity
Biological ProcessD-ribose catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribokinase
  • EC number
  • Short names
    RK

Gene names

    • ORF names
      B7P43_G05805

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Polyneoptera > Dictyoptera > Blattodea > Blattoidea > Termitoidae > Kalotermitidae > Cryptotermitinae > Cryptotermes

Accessions

  • Primary accession
    A0A2J7PNA5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-110Carbohydrate kinase PfkB
Domain121-245Carbohydrate kinase PfkB

Sequence similarities

Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.
Belongs to the carbohydrate kinase pfkB family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    255
  • Mass (Da)
    26,951
  • Last updated
    2018-03-28 v1
  • Checksum
    3B5A3F5116E02FE0
MNSKIVVIGSCNIDLQCFTPRLPRPGETLHGTEFRKGFGGKGANQCVAAAKLGSSTAMIARLGNDSFGQEFHRALKDNKINTDYVLMTDGVSSGLALITVAQNGIAIVNAAPAVTNPDPLVFRLSDIFCVNESEAEVLTGMAVQSVDEAKVAVGLLLDKGCKQVIITLGASGAVFASQGNLTPVHVPTKTVKSVDSTGAGDMFVGGLAFYLAYYPQLPMREIVKRSCEVATVSVQNYGTQTSFPTKDDLPTELFL

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2J7PN96A0A2J7PN96_9NEOPB7P43_G05805198

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NEVH01023955
EMBL· GenBank· DDBJ
PNF17811.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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